Literature DB >> 11048743

Determination of ionization efficiency of glycated and non-glycated peptides from the N-terminal of hemoglobin beta-chain by electrospray ionization mass spectrometry.

T Nakanishi1, A Shimizu.   

Abstract

We compared the ionization efficiency of glycated and non-glycated peptides for the HbA1c measurement method developed by Kobold et al. [Clin. Chem., 43 (1997) 1944] based on LC-ESI-MS analysis of the N-terminal peptides of the beta-chains released by cleavage of the hemoglobin with endoproteinase Glu-C. Taking half the peak area of the doubly charged ion and adding it to the area of the singly charged ion, we determined that the slope of the resulting calibration curve was nearly equal to 1, and the reproducibility of the added values was better than the values calculated by the doubly or the singly charged ion alone.

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Year:  2000        PMID: 11048743     DOI: 10.1016/s0378-4347(00)00115-8

Source DB:  PubMed          Journal:  J Chromatogr B Biomed Sci Appl        ISSN: 1387-2273


  2 in total

1.  A method to determine the ionization efficiency change of peptides caused by phosphorylation.

Authors:  Yuan Gao; Yinsheng Wang
Journal:  J Am Soc Mass Spectrom       Date:  2007-08-22       Impact factor: 3.109

2.  Electrospray ionisation mass spectrometry: principles and clinical applications.

Authors:  C S Ho; C W K Lam; M H M Chan; R C K Cheung; L K Law; L C W Lit; K F Ng; M W M Suen; H L Tai
Journal:  Clin Biochem Rev       Date:  2003
  2 in total

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